In our laboratory, we have generated a catalytic antibody that cleaves the phenyl ester of n-formyl norleucine stereoselectively and with a high efficiency. This antibody also possesses several characteristics found in catalysts that nature has evolved. The characteristics include the use of active site amino acids to participate in bond order changes, and the use o f binding interactions that are relatively remote from the reactive center to help promote catalysis. In this project we are studing how this antibody uses these remote binding interactions to promote catalysis. These interactions are very interesting because most of hapten design has been geared towards manipulating the active site close to the reactive center; there have been no investigations as to how these remote type of binding interaction can influence the catalytic mechanism of catalytic antibodies. We are using the graphics in the Computer Graphics Laboratory to visualize models of the catalytic antibody generated in our lab as well as those generated in other labs (and natural enzymes) to assist in guiding site- directed mutagenesis, and other protein engineering studies. Being able to use these structure is also instrumental in helping us understand the structural basis of antibody catalysis as well as protein based catalysis in general.